3ZFN
Crystal structure of product-like, processed N-terminal protease Npro
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-09 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.390, 41.160, 44.300 |
| Unit cell angles | 90.00, 115.38, 90.00 |
Refinement procedure
| Resolution | 28.710 - 1.500 |
| R-factor | 0.17303 |
| Rwork | 0.170 |
| R-free | 0.23883 |
| Structure solution method | MAD |
| Starting model (for MR) | SEMET-SUBSTITUTED PROTEIN |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.111 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.540 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.050 | 0.210 |
| Number of reflections | 21445 | |
| <I/σ(I)> | 15 | 5.2 |
| Completeness [%] | 96.5 | 95.3 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 100MM NA ACETATE, PH8.5 50% PEG6000 |
